Enzymes
| UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
- Name help_outline (2E,6E)-farnesyl diphosphate Identifier CHEBI:175763 Charge -3 Formula C15H25O7P2 InChIKeyhelp_outline VWFJDQUYCIWHTN-YFVJMOTDSA-K SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\C(C)=C\COP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 175 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-tryptophyl-[protein]
Identifier
RHEA-COMP:15365
Reactive part
help_outline
- Name help_outline L-tryptophan residue Identifier CHEBI:29954 Charge 0 Formula C11H10N2O SMILEShelp_outline C1(=CNC2=C1C=CC=C2)C[C@@H](C(=O)*)N* 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
(2S,3R)-3-farnesyl-2,3-dihydro-2,Nα-cyclo-L-tryptophyl-[protein]
Identifier
RHEA-COMP:17488
Reactive part
help_outline
- Name help_outline (2S,3R)-3-farnesyl-2,3-dihydro-2,Nα-cyclo-L-tryptophan residue Identifier CHEBI:177368 Charge 0 Formula C26H34N2O SMILEShelp_outline C1=2N[C@]3([C@@](C1=CC=CC2)(C[C@@H](C(=O)*)N3*)C/C=C(/CC/C=C(\C)/CCC=C(C)C)\C)[H] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,129 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:68384 | RHEA:68385 | RHEA:68386 | RHEA:68387 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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A tryptophan prenyltransferase with broad substrate tolerance from Bacillus subtilis subsp. natto.
Sugita T., Okada M., Nakashima Y., Tian T., Abe I.
Bacillus subtilis subsp. natto secretes the ComX<sub>natto</sub> pheromone as a quorum-sensing pheromone to produce poly-γ-glutamate for biofilm formation. The amino-acid sequence of the pheromone is Lys-Trp-Pro-Pro-Ile-Glu, and the tryptophan residue is post-translationally modified with a farnes ... >> More
Bacillus subtilis subsp. natto secretes the ComX<sub>natto</sub> pheromone as a quorum-sensing pheromone to produce poly-γ-glutamate for biofilm formation. The amino-acid sequence of the pheromone is Lys-Trp-Pro-Pro-Ile-Glu, and the tryptophan residue is post-translationally modified with a farnesyl group to form a tricyclic scaffold. Unlike other Bacillus ComX pheromones, the tryptophan residue is distant from the C-terminal end of the precursor peptide ComX<sub>natto</sub> . Here, we report the functional analysis of ComQ<sub>natto</sub> , which catalyzes a unique farnesyl-transfer reaction. ComQ<sub>natto</sub> recognizes not only full-length ComX<sub>natto</sub> but also N-and/or C-terminal truncated ComX<sub>natto</sub> analogues and even a single tryptophan for modification with a farnesyl group in vitro. These results, together with the calculated kinetic parameters, suggest that ComQ<sub>natto</sub> does not require a leader sequence for substrate recognition and is a promising enzyme with broad substrate tolerance for the synthesis of various prenylated tryptophan derivatives. << Less
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Identification of critical residues for the catalytic activity of ComQ, a Bacillus prenylation enzyme for quorum sensing, by using a simple bioassay system.
Hirooka K., Shioda S., Okada M.
<i>Bacillus</i> ComQ participates in the biosynthesis of a quorum-sensing signaling molecule (ComX pheromone) through catalyzing the prenylation at a Trp residue of the precursor peptide (pre-ComX) with geranyl diphosphate (C<sub>10</sub> type) or farnesyl diphosphate (C<sub>15</sub> type). We hyp ... >> More
<i>Bacillus</i> ComQ participates in the biosynthesis of a quorum-sensing signaling molecule (ComX pheromone) through catalyzing the prenylation at a Trp residue of the precursor peptide (pre-ComX) with geranyl diphosphate (C<sub>10</sub> type) or farnesyl diphosphate (C<sub>15</sub> type). We hypothesized that several residues specifically conserved among either type of ComQs are important for their substrate specificities. Using a simple bioassay, we revealed that Phe63, Asn186, and Gly190 in ComQ<sub>RO-E-2</sub> (C<sub>10</sub> type) were nondisplaceable to Ser63, Gly186, and Val190, the corresponding residues in the C<sub>15</sub>-type ComQ, respectively. A three-dimensional model suggested that the 186th and 190th residues are involved in the pre-ComX binding. <i>In vitro</i> analysis showed that substitution of Phe63 with Ser in ComQ<sub>RO-E-2</sub> significantly reduced the geranylation activity but substantially enhanced the farnesylation activity, whereas substitution of Ser63 with Phe in ComQ<sub>168</sub> (C<sub>15</sub> type) reduced the farnesylation activity. Therefore, the 63rd residue was found to be significant for the prenyl-substrate preference.<b>Abbreviations:</b> GPP: geranyl diphosphate; FPP: farnesyl diphosphate; IPP: isopentenyl diphosphate; GGPP: geranylgeranyl diphosphate; FARM: first aspartate-rich motif; SARM: second aspartate-rich motif; β-Gal: β-galactosidase; TBABG: tryptose blood agar base supplemented with glucose; X-gal: 5-bromo-4-chloro-3-indolyl-β-D-galactoside. << Less
Biosci. Biotechnol. Biochem. 84:347-357(2020) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.